GA201: A Novel Humanized and Glycoengineered Anti-EGFR Antibody—Response

@article{Gerdes2014GA201AN,
  title={GA201: A Novel Humanized and Glycoengineered Anti-EGFR Antibody—Response},
  author={Christian A. Gerdes and Pablo Uma{\~n}a},
  journal={Clinical Cancer Research},
  year={2014},
  volume={20},
  pages={1055 - 1055}
}
We are pleased that Dr. Modjtahedi found our work on GA201 interesting. The origin of the CDR sequences of GA201 based on the published sequences of the ICR62 antibody is clearly mentioned in our publication ([1][1]). Likewise, previous publications describing the properties of ICR62 were also cited 

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GA201 (RG7160): A Novel, Humanized, Glycoengineered Anti-EGFR Antibody with Enhanced ADCC and Superior In Vivo Efficacy Compared with Cetuximab
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A detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC is obtained and a unique mechanism by which the immune system can regulate antibody-mediated effector functions is suggested.
Br€ unker P, Uma~ na P. The carbohydrate at FcgRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
  • J Biol Chem
  • 2006
Authors' Affiliation: Roche Glycart AG, pRED